1pxd

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(New page: 200px<br /><applet load="1pxd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pxd, resolution 1.8&Aring;" /> '''Crystal structure of ...)
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[[Image:1pxd.gif|left|200px]]<br /><applet load="1pxd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pxd, resolution 1.8&Aring;" />
caption="1pxd, resolution 1.8&Aring;" />
'''Crystal structure of the complex of jacalin with meso-tetrasulphonatophenylporphyrin.'''<br />
'''Crystal structure of the complex of jacalin with meso-tetrasulphonatophenylporphyrin.'''<br />
==Overview==
==Overview==
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The crystal structure of the complex of meso-tetrasulfonatophenylporphyrin, (H(2)TPPS) with jack fruit (Artocarpus integriflora) agglutinin (jacalin), has been determined at 1.8 A resolution. A porphyrin pair is sandwiched, between two symmetry-related jacalin monomers in the crystal, leading to a, cross-linking network of protein molecules. Apart from the stacking, interactions, H(2)TPPS also forms hydrogen bonds, some involving water, bridges, with jacalin at the carbohydrate-binding site. The residues that, are involved in rendering galactopyranoside specificity to jacalin undergo, conformational adjustments in order to accommodate the H(2)TPPS molecule., The water molecules at the carbohydrate-binding site of jacalin cement the, jacalin-porphyrin interactions, optimizing their complementarity., Interactions of porphyrin with jacalin are relatively weak compared with, those observed between galactopyranoside and jacalin, perhaps because the, former largely involves water-mediated hydrogen bonds. While H(2)TPPS, binds to jacalin at the carbohydrate-binding site as in the case of ConA, its mode of interaction with jacalin is very different. H(2)TPPS does not, enter the carbohydrate-binding cavity of jacalin. Instead, it sits over, the binding site. While the porphyrin binding is mediated by replicating, the hydrogen-bonding network of mannopyranoside through the sulfonate, atoms in the case of ConA, the plasticity associated with the, carbohydrate-binding site accommodates the pluripotent porphyrin molecule, in the case of jacalin through an entirely different set of interactions.
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The crystal structure of the complex of meso-tetrasulfonatophenylporphyrin (H(2)TPPS) with jack fruit (Artocarpus integriflora) agglutinin (jacalin) has been determined at 1.8 A resolution. A porphyrin pair is sandwiched between two symmetry-related jacalin monomers in the crystal, leading to a cross-linking network of protein molecules. Apart from the stacking interactions, H(2)TPPS also forms hydrogen bonds, some involving water bridges, with jacalin at the carbohydrate-binding site. The residues that are involved in rendering galactopyranoside specificity to jacalin undergo conformational adjustments in order to accommodate the H(2)TPPS molecule. The water molecules at the carbohydrate-binding site of jacalin cement the jacalin-porphyrin interactions, optimizing their complementarity. Interactions of porphyrin with jacalin are relatively weak compared with those observed between galactopyranoside and jacalin, perhaps because the former largely involves water-mediated hydrogen bonds. While H(2)TPPS binds to jacalin at the carbohydrate-binding site as in the case of ConA, its mode of interaction with jacalin is very different. H(2)TPPS does not enter the carbohydrate-binding cavity of jacalin. Instead, it sits over the binding site. While the porphyrin binding is mediated by replicating the hydrogen-bonding network of mannopyranoside through the sulfonate atoms in the case of ConA, the plasticity associated with the carbohydrate-binding site accommodates the pluripotent porphyrin molecule in the case of jacalin through an entirely different set of interactions.
==About this Structure==
==About this Structure==
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1PXD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Artocarpus_integer Artocarpus integer] with SFP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PXD OCA].
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1PXD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Artocarpus_integer Artocarpus integer] with <scene name='pdbligand=SFP:'>SFP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXD OCA].
==Reference==
==Reference==
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[[Category: Anuradha, P.]]
[[Category: Anuradha, P.]]
[[Category: Goel, M.]]
[[Category: Goel, M.]]
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[[Category: Kaur, K.J.]]
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[[Category: Kaur, K J.]]
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[[Category: Maiya, B.G.]]
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[[Category: Maiya, B G.]]
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[[Category: Salunke, D.M.]]
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[[Category: Salunke, D M.]]
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[[Category: Swamy, M.J.]]
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[[Category: Swamy, M J.]]
[[Category: SFP]]
[[Category: SFP]]
[[Category: lectin]]
[[Category: lectin]]
[[Category: porphyrin]]
[[Category: porphyrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:12:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:32 2008''

Revision as of 12:33, 21 February 2008


1pxd, resolution 1.8Å

Drag the structure with the mouse to rotate

Crystal structure of the complex of jacalin with meso-tetrasulphonatophenylporphyrin.

Overview

The crystal structure of the complex of meso-tetrasulfonatophenylporphyrin (H(2)TPPS) with jack fruit (Artocarpus integriflora) agglutinin (jacalin) has been determined at 1.8 A resolution. A porphyrin pair is sandwiched between two symmetry-related jacalin monomers in the crystal, leading to a cross-linking network of protein molecules. Apart from the stacking interactions, H(2)TPPS also forms hydrogen bonds, some involving water bridges, with jacalin at the carbohydrate-binding site. The residues that are involved in rendering galactopyranoside specificity to jacalin undergo conformational adjustments in order to accommodate the H(2)TPPS molecule. The water molecules at the carbohydrate-binding site of jacalin cement the jacalin-porphyrin interactions, optimizing their complementarity. Interactions of porphyrin with jacalin are relatively weak compared with those observed between galactopyranoside and jacalin, perhaps because the former largely involves water-mediated hydrogen bonds. While H(2)TPPS binds to jacalin at the carbohydrate-binding site as in the case of ConA, its mode of interaction with jacalin is very different. H(2)TPPS does not enter the carbohydrate-binding cavity of jacalin. Instead, it sits over the binding site. While the porphyrin binding is mediated by replicating the hydrogen-bonding network of mannopyranoside through the sulfonate atoms in the case of ConA, the plasticity associated with the carbohydrate-binding site accommodates the pluripotent porphyrin molecule in the case of jacalin through an entirely different set of interactions.

About this Structure

1PXD is a Protein complex structure of sequences from Artocarpus integer with as ligand. Full crystallographic information is available from OCA.

Reference

Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction., Goel M, Anuradha P, Kaur KJ, Maiya BG, Swamy MJ, Salunke DM, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):281-8. Epub 2004, Jan 23. PMID:14747704

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